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O77263 (TRMB_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA (guanine-N(7)-)-methyltransferase

EC=2.1.1.33
Alternative name(s):
tRNA (guanine(46)-N(7))-methyltransferase
tRNA(m7G46)-methyltransferase
Gene names
ORF Names:CG4045
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA By similarity. HAMAP-Rule MF_03055

Catalytic activity

S-adenosyl-L-methionine + guanine46 in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine46 in tRNA. HAMAP-Rule MF_03055

Pathway

tRNA modification; N(7)-methylguanine-tRNA biosynthesis. HAMAP-Rule MF_03055

Subcellular location

Nucleus By similarity HAMAP-Rule MF_03055.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentNucleus
   LigandRNA-binding
S-adenosyl-L-methionine
tRNA-binding
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA (guanine-N7)-methylation

Inferred from sequence or structural similarity. Source: GOC

tRNA modification

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiontRNA (guanine-N7-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 256256tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_03055
PRO_0000171434

Regions

Region102 – 1032S-adenosyl-L-methionine binding By similarity
Region137 – 1382S-adenosyl-L-methionine binding By similarity
Region235 – 2373S-adenosyl-L-methionine binding By similarity

Sites

Active site1601 By similarity
Binding site791S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1571S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
O77263 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 9E0F0B8AC97FC00E

FASTA25629,425
        10         20         30         40         50         60 
MVATGGQAQD QGQNQEPDVL NPTSAVTGLP QKRYYRQRAH SNPIADHSFD YPARPEDVDW 

        70         80         90        100        110        120 
RSMYPGIQQG QQVSFADIGC GYGGFLVTLG EMFPEKLSIG MEIRVKVSDY VVDRIAALRR 

       130        140        150        160        170        180 
RCADTGAYQN IACLRTNAMK YLPNYFVKGQ LEKMFFLYPD PHFKRAKHKW RIINQALLSE 

       190        200        210        220        230        240 
YAYILRKGGL LYTMTDVEDL HKWIVTHMEE HPLYERLTEE EANADPITPK LYQSSEEGAK 

       250 
VVRNKGDHFL AIFRRL 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"From sequence to chromosome: the tip of the X chromosome of D. melanogaster."
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. expand/collapse author list , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M.
Science 287:2220-2222(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Oregon-R.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Ovary.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014298 Genomic DNA. Translation: AAF45720.2.
AL031765 Genomic DNA. Translation: CAA21130.1.
AY094742 mRNA. Translation: AAM11095.1.
PIRT13746.
RefSeqNP_569978.1. NM_130622.3.
UniGeneDm.26191.

3D structure databases

ProteinModelPortalO77263.
SMRO77263. Positions 51-256.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid57720. 2 interactions.
DIPDIP-18791N.
IntActO77263. 2 interactions.
MINTMINT-932740.
STRING7227.FBpp0070317.

Proteomic databases

PaxDbO77263.
PRIDEO77263.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0070331; FBpp0070317; FBgn0025629.
GeneID31176.
KEGGdme:Dmel_CG4045.
UCSCCG4045-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0025629. CG4045.

Phylogenomic databases

eggNOGCOG0220.
GeneTreeENSGT00390000017840.
InParanoidO77263.
KOK03439.
OMARAHSNPI.
OrthoDBEOG7PS1GC.
PhylomeDBO77263.

Enzyme and pathway databases

UniPathwayUPA00989.

Gene expression databases

BgeeO77263.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
HAMAPMF_03055. tRNA_methyltr_TrmB_euk.
InterProIPR029063. SAM-dependent_MTases-like.
IPR025763. Trm8_euk.
IPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]
PfamPF02390. Methyltransf_4. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
TIGRFAMsTIGR00091. TIGR00091. 1 hit.
PROSITEPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi31176.
NextBio772318.
PROO77263.

Entry information

Entry nameTRMB_DROME
AccessionPrimary (citable) accession number: O77263
Secondary accession number(s): Q9W527
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase